ArticleNature2013
Structure of the human glucagon class B G-protein-coupled receptor.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 172 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
172 citing papers in PubMed, 373 citations in OpenAlex.
- Glucagon and GLP-1 in hemodialysis: associations with mortality and nutritional decline.International urology and nephrology · 2026Article
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- Glucagon Can Increase Force of Contraction via Glucagon Receptors in the Isolated Human Atrium.International journal of molecular sciences · 2025Article
- Identification of Small-Molecule Antagonists Targeting the Growth Hormone Releasing Hormone Receptor (GHRHR).Journal of chemical information and modeling · 2024Article
- Insights on the G protein-coupled receptor helix 8 solution structure and orientation using a neurotensin receptor 1 peptide.Protein science : a publication of the Protein Society · 2024Article
- Crystallization of Ethylene Plant Hormone Receptor-Screening for Structure.Biomolecules · 2024Article
- The Role of G Protein-Coupled Receptors and Receptor Kinases in PancreaticPharmacological reviews · 2024Review
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- Article
- Discovery of MK-1462: GLP-1 and Glucagon Receptor Dual Agonist for the Treatment of Obesity and Diabetes.ACS medicinal chemistry letters · 2022Article
- Discovery of Insulin/GLP-1/Glucagon Triagonists for the Treatment of Diabetes and Obesity.ACS medicinal chemistry letters · 2022Article
- Targeting VIP and PACAP Receptor Signaling: New Insights into Designing Drugs for the PACAP Subfamily of Receptors.International journal of molecular sciences · 2022Review
- GPCR Intracellular Loop Regulation of Beta-Arrestin-Mediated Endosomal Signaling Dynamics.Journal of molecular neuroscience : MN · 2022Article
- Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors.Nature communications · 2022Article
- Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation.Nature communications · 2022Article
- The Evolutionary History of Vertebrate Adhesion GPCRs and Its Implication on Their Classification.International journal of molecular sciences · 2021Article
- Ligand-Receptor Interactions and Machine Learning in GCGR and GLP-1R Drug Discovery.International journal of molecular sciences · 2021Article
- The Effects of Sodium Ions on Ligand Binding and Conformational States of G Protein-Coupled Receptors-Insights from Mass Spectrometry.Journal of the American Chemical Society · 2021Article
- The Role of ICL1 and H8 in Class B1 GPCRs; Implications for Receptor Activation.Frontiers in endocrinology · 2021Article
- Molecular Basis of Class B GPCR Selectivity for the Neuropeptides PACAP and VIP.Frontiers in molecular biosciences · 2021Article
112 more citing papers are in PubMed but not listed here.
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Authors and funding
16 authors at 6 institutions in 4 countries.
Funding
Abstract
Binding of the glucagon peptide to the glucagon receptor (GCGR) triggers the release of glucose from the liver during fasting; thus GCGR plays an important role in glucose homeostasis. Here we report the crystal structure of the seven transmembrane helical domain of human GCGR at 3.4 Å resolution, complemented by extensive site-specific mutagenesis, and a hybrid model of glucagon bound to GCGR to understand the molecular recognition of the receptor for its native ligand. Beyond the shared seven transmembrane fold, the GCGR transmembrane domain deviates from class A G-protein-coupled receptors with a large ligand-binding pocket and the first transmembrane helix having a 'stalk' region that extends three alpha-helical turns above the plane of the membrane. The stalk positions the extracellular domain (~12 kilodaltons) relative to the membrane to form the glucagon-binding site that captures the peptide and facilitates the insertion of glucagon's amino terminus into the seven transmembrane domain.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.